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Probable ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase)

 A7AUF6_BABBO            Unreviewed;      1337 AA.
A7AUF6;
11-SEP-2007, integrated into UniProtKB/TrEMBL.
11-SEP-2007, sequence version 1.
25-OCT-2017, entry version 54.
RecName: Full=Probable ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03185};
Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03185};
Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03185};
EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03185};
AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03185};
ORFNames=BBOV_II006170 {ECO:0000313|EMBL:EDO06567.1};
Babesia bovis.
Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
Babesiidae; Babesia.
NCBI_TaxID=5865 {ECO:0000313|EMBL:EDO06567.1, ECO:0000313|Proteomes:UP000002173};
[1] {ECO:0000313|EMBL:EDO06567.1, ECO:0000313|Proteomes:UP000002173}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=T2Bo {ECO:0000313|EMBL:EDO06567.1,
ECO:0000313|Proteomes:UP000002173};
PubMed=17953480; DOI=10.1371/journal.ppat.0030148;
Brayton K.A., Lau A.O.T., Herndon D.R., Hannick L., Kappmeyer L.S.,
Berens S.J., Bidwell S.L., Brown W.C., Crabtree J., Fadrosh D.,
Feldblum T., Forberger H.A., Haas B.J., Howell J.M., Khouri H.,
Koo H., Mann D.J., Norimine J., Paulsen I.T., Radune D., Ren Q.,
Smith R.K. Jr., Suarez C.E., White O., Wortman J.R., Knowles D.P. Jr.,
McElwain T.F., Nene V.M.;
"Genome sequence of Babesia bovis and comparative analysis of
apicomplexan hemoprotozoa.";
PLoS Pathog. 3:1401-1413(2007).
-!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
to fructose 1,6-bisphosphate by ATP, the first committing step of
glycolysis. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_03185};
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000256|HAMAP-Rule:MF_03185}.
-!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta
(catalytic) chains. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. PPi-dependent PFK group II subfamily. Clade "Long" sub-
subfamily. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EDO06567.1}.
-----------------------------------------------------------------------
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EMBL; AAXT01000003; EDO06567.1; -; Genomic_DNA.
RefSeq; XP_001610135.1; XM_001610085.1.
ProteinModelPortal; A7AUF6; -.
EnsemblProtists; EDO06567; EDO06567; BBOV_II006170.
GeneID; 5478369; -.
KEGG; bbo:BBOV_II006170; -.
EuPathDB; PiroplasmaDB:BBOV_II006170; -.
InParanoid; A7AUF6; -.
KO; K00895; -.
OMA; CCSIRGL; -.
UniPathway; UPA00109; UER00182.
Proteomes; UP000002173; Partially assembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR011183; PfpB_PPi_PFK.
InterPro; IPR000023; Phosphofructokinase_dom.
InterPro; IPR035966; PKF_sf.
Pfam; PF00365; PFK; 2.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 2.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03185};
Complete proteome {ECO:0000313|Proteomes:UP000002173};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_03185};
Kinase {ECO:0000256|HAMAP-Rule:MF_03185, ECO:0000313|EMBL:EDO06567.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_03185};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03185};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03185};
Reference proteome {ECO:0000313|Proteomes:UP000002173};
Transferase {ECO:0000256|HAMAP-Rule:MF_03185,
ECO:0000313|EMBL:EDO06567.1}.
DOMAIN 192 446 PFK. {ECO:0000259|Pfam:PF00365}.
DOMAIN 773 1011 PFK. {ECO:0000259|Pfam:PF00365}.
NP_BIND 264 265 ATP. {ECO:0000256|HAMAP-Rule:MF_03185}.
NP_BIND 293 296 ATP. {ECO:0000256|HAMAP-Rule:MF_03185}.
REGION 334 336 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03185}.
REGION 381 383 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03185}.
REGION 544 547 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03185}.
ACT_SITE 336 336 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_03185}.
METAL 294 294 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03185}.
BINDING 200 200 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03185}.
BINDING 442 442 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03185}.
SITE 295 295 Important for substrate specificity;
cannot use PPi as phosphoryl donor.
{ECO:0000256|HAMAP-Rule:MF_03185}.
SEQUENCE 1337 AA; 149622 MW; EFB83CA2097A8DAF CRC64;
MMEEKVGRGS GEDGDMRMVR MVSAESICGD KSCQSPASSV ELDMRDFVDD DFERRRKRYQ
LNKSFNTFRR CATRQPDHDS FTSLPGIKHN TAEFSYPINP FVNKKDGDRI KRVNSCYISK
SVCQGLYRNR DVELPTLLQY DFHLLDEHDE SGEELRDFDE LSSVLSHIAH NKMVSVAPQM
LATSVTSHPI IKIGMVLSGG PAPGGHNVIA GVFDYLYLRN TQSQLIGFHG GLDGLFGRHH
EVVTPEVMDN FRNMGGFNMF LSGRGRINGP EDLDRVVEAV NDLDLDGLII VGGDGSNSNA
ALLANHMAYR FGCDSSDGRP VLRKRCCVIG IPKTVDGDVQ SHNIEVSFGF DTAARTYSEL
IGNLCTDASS TQYTYHFIRV MGRSASHLAL ECGMQTHPNI VLIGEEAQSK QQSLSMIVDY
IVDLMEKRYQ MGKPYGVVLI PEGLIEFIPE INVLISELNE ILVQAKGPIT HLDPSCLTKS
RATWEILPDT IREQLLMDRE ATGYVMLAKI ATERLLLMLV EARIAERKLS HLSSLRFMTH
YFGYEGRCAM PSDFDGAYCY SLGYNAGVLI SAKRNGYMSV IRDLKAPISE WIPLGVPFLH
LMHMINLGGK RAPAIRKTLL NLDGKLFKTF EKVREIWAYN DLYRSPGPIQ LFNSDYQRCF
SISDPQVEDL IGSFKEAPAE KSRFLLHRNL ECMSPLQLSR LEWRPPIPML CHDPRARMRN
FKEVHSNDSY TRDQVALNYP YMTRRSHFSL HEVVGHYSGD RTNLNKATQG LRVGVVLLSK
QAPGVLNVIW GIHERMSIIG GSCVAFHGAL GLIEGNYIEL TSSDFDTFRN QGGLDMIHRS
RVQYFQEPKN WSLALETCTQ LGLNALIILG DEFAMTQGAL LTEYFLSQQS SICVIGVPVA
GSNSLAGPLI ESCVGFDSNA QLYASLVGNV LTDAVSMPKY WHFVKILGRY PSLEVLECAL
QTHPNVIIIA EEYGSADKTL FDVVRDIADA VCKRAAMGKN YGTVLIPDHL ILHLPNTKSM
LMELRSVLME ASAANKRREA VDSFLNYDKS EPQSSEWINK MTPWSLGVFG SLPLYIRKEV
LNFDMEVALE RLDIEIMLSK MVKEELNLRK ATGAYKGNYA AVTHYFGYQG RCCTPSEFDC
SLAFAYGHVA SIAAESGLTG VCCSIRGLCG EIEAWKMYAV PLTCLMKVEP NIMTPISLND
FKKGELPMVP SSTVSLKSKA FRKLSMARKK WLVEDLFINP GPIQFDGIVT AQSMVLITEH
AEYYQMLHSV ERFLNVLQNT CKFGVSEEYL NHAFVQLWGL LKVSQSPGDL VRIAEMLKAE
EDNSLRSTGN AFSLSSF


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